来自橄榄绿链霉菌E-86的G/11家族β-木聚糖酶的纯化与特性分析

Purification and characterization of a family G/11 beta-xylanase from Streptomyces olivaceoviridis E-86.

作者信息

Kaneko S, Kuno A, Muramatsu M, Iwamatsu S, Kusakabe I, Hayashi K

机构信息

National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, Ibaraki, Japan.

出版信息

Biosci Biotechnol Biochem. 2000 Feb;64(2):447-51. doi: 10.1271/bbb.64.447.

DOI:10.1271/bbb.64.447

PMID:10737210

Abstract

A beta-xylanase (GXYN) was purified from the culture filtrate of Streptomyces olivaceoviridis E-86 by successive chromatography on DE-52, CM-Sepharose and Superose 12. The molecular mass of the xylanase was estimated to be 23 kDa, indicating that the enzyme consists of a catalytic domain only. The enzyme displayed an optimum pH of 6, a temperature optimum of 60 degrees C, a pH stability range from 2 to 11 and thermal stability up to 40 degrees C. The N-terminal amino acid sequence of GXYN was A-T-V-I-T-T-N-Q-T-G-T-N-N-G-I-Y-Y-S-F-W-, and sharing a high degree of similarity with the N-terminal sequence of xylanases B and C from Streptomyces lividans, indicating GXYN belongs to family G/11 of glycoside hydrolases. GXYN was inferior to xylanase B from Streptomyces lividans in the hydrolysis of insoluble xylan because of its lack of a xylan binding domain.

摘要

通过在DE - 52、CM - 琼脂糖凝胶和Superose 12上连续层析，从橄榄绿链霉菌E - 86的培养滤液中纯化出一种β - 木聚糖酶（GXYN）。该木聚糖酶的分子量估计为23 kDa，表明该酶仅由一个催化结构域组成。该酶的最适pH为6，最适温度为60℃，pH稳定范围为2至11，热稳定性高达40℃。GXYN的N端氨基酸序列为A - T - V - I - T - T - N - Q - T - G - T - N - N - G - I - Y - Y - S - F - W - ，与产色链霉菌木聚糖酶B和C的N端序列具有高度相似性，表明GXYN属于糖苷水解酶家族G/11。由于缺乏木聚糖结合结构域，GXYN在不溶性木聚糖的水解方面不如产色链霉菌的木聚糖酶B。